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Role of Bacteria in Urinary Tract Infections
Published in K. Balamurugan, U. Prithika, Pocket Guide to Bacterial Infections, 2019
JebaMercy Gnanasekaran, Kannan Balaji, K. Balamurugan
The ability of S. aureus to cause a wide spectrum of disease has been attributed to its ability to produce a broad array of pathogenicity factors. These factors can be subdivided into three general groups: cell-associated products, secreted exoproteins, and regulatory loci. Cell-associated products, including adhesins of the microbial surface components recognizing adhesive matrix molecules (MSCRAMM) family and capsular polysaccharide, facilitate binding to host tissue and help resist host immune responses. The exoproteins like cytolysins and extracellular proteases are known to fight against host immunity and results in tissue invasion and nutrient absorbance (Lowy et al., 1998; Sifri et al., 2003).
Enterococcus: An Important Opportunistic Pathogen—Basic and Clinical Aspects
Published in Dongyou Liu, Handbook of Foodborne Diseases, 2018
Karen Flores-Moreno, Claudia Mayoral-Teran, Yolanda Lopez-Vidal
E. faecium adhesion protein. E. faecium presents adhesion proteins, as does E. faecalis. One of the proteins present in E. faecium is Acm. The Acm protein is an adhesin that binds primarily to type I collagen, although it may also bind to collagen types IV to a lesser extent. In an analysis of the genome of the E. faecium TX16 (DO) strain, the acm gene encoding the MSCRAMM family of proteins was identified with the greatest similarity to S. aureus. Its expression has been related to clinical isolates that cause endocarditis with vegetation formation.
Host–Biofilm Interactions at Mucosal Surfaces and Implications in Human Health
Published in Chaminda Jayampath Seneviratne, Microbial Biofilms, 2017
Nityasri Venkiteswaran, Kassapa Ellepola, Chaminda Jayampath Seneviratne, Yuan Kun Lee, Kia Joo Puan, Siew Cheng Wong
Recent reports by Kang et al. have demonstrated that MSCRAMM of some Gram-positive bacteria can inhibit complement activation of the classical pathway by targeting C1q [166]. Biofilm bacteria of P. aeruginosa do not trigger oxidative bursts of polymorphonuclear leukocytes (PMNs) to the same degree as that of planktonic bacteria, thereby halting the activation of immune cells [167–169]. In addition, P. aeruginosa biofilms produce the exopolysaccharide alginate, which protects the bacteria from being killed by macrophages [170]. Alginate has also been shown to induce conformational changes to AMP and cause aggregation of the AMP, preventing access to the cytoplasmic membrane [171].
The distinct effects of aspirin on platelet aggregation induced by infectious bacteria
Published in Platelets, 2020
Nadji Hannachi, Jean-Pierre Baudoin, Arsha Prasanth, Gilbert Habib, Laurence Camoin-Jau
Several bacterial strains, such as staphylococci, streptococci, and enterococci play pivotal roles in the etiology of IE [5,6]. These roles are based on the presence of proteins and/or receptors on the surface of these bacteria that directly or indirectly interact with platelets. S. aureus is currently considered to be the main causative agent of IE [5]. S. aureus expresses surface proteins belonging to the microbial surface components that recognize the family of adhesive matrix molecules (MSCRAMM) such as clumping factor (ClfA and ClfB) and fibronectin-binding protein (Fnbp A and FnbpB). These molecules allow bacteria to adhere to tissues and induce platelet aggregation [3,7]. Furthermore, because of the presence of coagulases, S. aureus contributes to the development of fibrino-platelet vegetation during staphylococcal endocarditis [7,8].
Emergence of coagulase-negative staphylococci
Published in Expert Review of Anti-infective Therapy, 2020
Karsten Becker, Anna Both, Samira Weißelberg, Christine Heilmann, Holger Rohde
An important family of staphylococcal cell wall-anchored (CWA) surface proteins mediating specific interactions with a variety of host structures are the microbial surface components recognizing adhesive matrix molecules (MSCRAMMs) [93]. MSCRAMMs have a common structural organization including a ligand-binding domain and a C-terminal LPXTG motif responsible for covalent linkage to the cell wall peptidoglycan [94,95]. As a prototype, the S. epidermidis serine (S)-aspartate (D) repeat (Sdr) protein SdrG (also termed Fbe) binds to Fg via the so-called ‘dock, lock, and latch’ mechanism that has been postulated from crystal structures [96,97]. SdrF is another S. epidermidis MSCRAMM that binds to collagen and contributes to driveline infections [98,99]. Recently, a novel MSCRAMM subfamily has been described in S. epidermidis with the prototype SesJ [100]. Some LPXTG-containing S. epidermidis surface (Ses) proteins may represent suitable targets in the vaccine development to prevent biofilm-associated infections, because respective antibodies were able to significantly reduce in vivo biofilm formation [101–104].